title: [Interaction between oxyhemoglobin and cytoplasmic fragments of band 3 protein purified from human erythrocyte membranes].
abstract: The cytoplasmic fragment of the band 3 protein strongly interacts with oxyhemoglobin, as shown by rate zonal centrifugation and fluorescence quenching measurements. According to their relative concentrations two different types of complexes can be formed with a molar ratio of the band 3 fragment per oxyhemoglobin tetramer of 0.9 and 1.8 respectively. The equilibrium binding constant of oxyhemoglobin for the peptide is 1.4 x 10(-7) M-1 in 5 mM phosphate buffer at pH 6. Glyceraldehyde-3-phosphate dehydrogenase or an increase in pH in ionic strength prevent this association.
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010108:Oxyhemoglobins / Q000378:metabolism*; D010446:Peptide Fragments / Q000097:blood; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D010108:Oxyhemoglobins; D010446:Peptide Fragments
vernacular_title: Etude de l'interaction entre l'oxyhémoglobine et le fragment cytoplasmique de la protéine "bande 3" purifiée des membranes des globules rouges humanis.